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Protein

CRISPR-associated endonuclease Cas1

Gene

ygbT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids) (PubMed:21255106, PubMed:24920831, PubMed:24793649). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The Cas1-Cas2 complex is involved in CRISPR adaptation, the first stage of CRISPR immunity, being required for the addition/removal of CRISPR spacers at the leader end of the CRISPR locus (PubMed:24920831, PubMed:25707795, PubMed:24793649). The Cas1-Cas2 complex introduces staggered nicks into both strands of the CRISPR array near the leader repeat and joins the 5'-ends of the repeat strands with the 3'-ends of the new spacer sequence (PubMed:24920831). Spacer DNA integration requires supercoiled target DNA and 3'-OH ends on the inserted (spacer) DNA and probably initiates with a nucleophilic attack of the C 3'-OH end of the protospacer on the minus strand of the first repeat sequence (PubMed:25707795). Expression of Cas1-Cas2 in a strain lacking both genes permits spacer acquisition (PubMed:24793649, PubMed:24920831). Non-specifically binds DNA; the Cas1-Cas2 complex preferentially binds CRISPR-locus DNA (PubMed:24793649). Highest binding is seen to a dual forked DNA complex with 3'-overhangs and a protospacer-adjacent motif-complement specifically positioned (PubMed:26478180). The protospacer DNA lies across a flat surface extending from 1 Cas1 dimer, across the Cas2 dimer and contacting the other Cas1 dimer; the 23 bp-long ds section of the DNA is bracketed by 1 Tyr-22 from each of the Cas1 dimers (PubMed:26478180, PubMed:26503043). Cas1 cuts within the 3'-overhang, to generate a 33-nucleotide DNA that is probably incorporated into the CRISPR leader by a cut-and-paste mechanism (PubMed:26478180). Cas1 alone endonucleolytically cleaves linear ssRNA, ssDNA and short (34 base) dsDNA as well as branched DNA substrates such as Holliday junctions, replication forks and 5'-flap DNA substrates (PubMed:21219465). In vitro catalyzes a concerted transesterification reaction on branched DNA, as would be expected during integration of protospacers into the CRISPR leader sequence; Cas2 is not required in vitro. This reaction requires a 3'-OH group at the branch point (PubMed:26284603). Genetic interactions suggest Cas1 interacts with components of the RecBC and RuvB DNA repair systems (PubMed:21219465).7 Publications

Cofactori

Mg2+3 PublicationsNote: Protospacer integration in vitro also occurs with Mn2+ and also requires low concentrations of KCl (PubMed:25707795). The transesterification function works equally well with Mg2+, Mn2+ or Co2+ in vitro (PubMed:26284603).2 Publications

Enzyme regulationi

Nuclease activity partially inhibited by CasE (PubMed:21219465).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei141 – 14112 Publications
Metal bindingi141 – 1411MagnesiumBy similarity
Active sitei208 – 20812 Publications
Metal bindingi208 – 2081MagnesiumBy similarity
Active sitei221 – 22112 Publications
Metal bindingi221 – 2211MagnesiumBy similarity

GO - Molecular functioni

  • 5'-flap endonuclease activity Source: EcoCyc
  • crossover junction endodeoxyribonuclease activity Source: EcoCyc
  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoCyc
  • defense response to virus Source: UniProtKB-HAMAP
  • DNA repair Source: UniProtKB-KW
  • maintenance of CRISPR repeat elements Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Antiviral defense, DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7425-MONOMER.
ECOL316407:JW2725-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CRISPR-associated endonuclease Cas1 (EC:3.1.-.-)
Gene namesi
Name:ygbT
Synonyms:cas1
Ordered Locus Names:b2755, JW2725
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13114. ygbT.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Not essential. Increased sensitivity to MMC and UV light; double ygbT-ruvA, ruvB or ruvC disruptions have no further phenotype suggesting Cas1 functions in the same DNA repair pathway (PubMed:21219465). Function in DNA repair also seems to require CRISPRs (PubMed:21219465). Cells elongate after 2 hours growth in MMC; they are even longer in double ygbT-ruvA, ruvB or ruvC disruptions, suggesting Cas1 may also function in chromosome segregation (PubMed:21219465). Loss of plasmid silencing (PubMed:21255106).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221Y → A: Slightly decreased spacer acquisition in vivo. 2 Publications
Mutagenesisi22 – 221Y → F: Nearly wild-type spacer acquisition in vivo. 1 Publication
Mutagenesisi41 – 411R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication
Mutagenesisi59 – 591R → A: Loss of spacer acquisition in vivo, decreased protospacer binding. 1 Publication
Mutagenesisi59 – 591R → D: Dramatically decreased spacer acquisition in vitro, 250-fold decreased affinity for protospacer DNA. 1 Publication
Mutagenesisi66 – 661R → D: Dramatically decreased spacer acquisition in vitro, 250-fold decreased affinity for protospacer DNA. 1 Publication
Mutagenesisi66 – 661R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication
Mutagenesisi84 – 841R → A: Decreased spacer acquisition in vivo. 1 Publication
Mutagenesisi84 – 841R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication
Mutagenesisi141 – 1411E → A: No cleavage of any substrates, no restoration of UV or mitomycin C (MMC) resistance (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649). 2 Publications
Mutagenesisi149 – 1491Y → A: No effect on in vitro protospacer integration. 1 Publication
Mutagenesisi165 – 1651Y → A: No effect on in vitro protospacer integration (PubMed:25707795). Alone significantly decreased protospacer acquisition in vivo (PubMed:26478180). Loss of protospacer acquisition, decreased protospacer binding; in association with A-170, significantly decreased protospacer binding; in association with A-217 (PubMed:26478180). 2 Publications
Mutagenesisi170 – 1701W → A: Alone significantly decreased protospacer acquisition in vivo (PubMed:26478180). Decreased protospacer binding; in association with A-170 (PubMed:26478180). 1 Publication
Mutagenesisi184 – 1841T → A: No cleavage of any substrates. 1 Publication
Mutagenesisi188 – 1881Y → A: Partial inhibition of cleavage (PubMed:21219465). No effect on in vitro protospacer integration (PubMed:25707795). Significantly decreased protospacer acquisition in vivo (PubMed:26478180). 3 Publications
Mutagenesisi208 – 2081H → A: No cleavage of any substrates, no restoration of UV or MMC resistance (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649, PubMed:25707795, PubMed:26478180). 4 Publications
Mutagenesisi211 – 2111K → A: No cleavage of any substrates. 1 Publication
Mutagenesisi217 – 2171Y → A: No effect on in vitro protospacer integration (PubMed:25707795). Alone significantly decreased protospacer acquisition in vivo (PubMed:26478180). Significantly decreased protospacer binding; in association with A-165 (PubMed:26478180). 2 Publications
Mutagenesisi218 – 2181D → A: No cleavage of any substrates, no restoration of UV or MMC resistance (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649). 2 Publications
Mutagenesisi221 – 2211D → A: No cleavage of any substrates (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649, PubMed:24920831, PubMed:25707795). No cleavage of CRISPR leader in preparation for spacer integration (PubMed:24920831). 4 Publications
Mutagenesisi224 – 2241K → A: No cleavage of any substrates (PubMed:21219465). Loss of spacer acquisition in vivo (PubMed:24793649, PubMed:25707795). 3 Publications
Mutagenesisi245 – 2484REVR → AEVA: Loss of spacer acquisition in vivo. 1 Publication
Mutagenesisi245 – 2451R → A: No effect on spacer acquisition. 1 Publication
Mutagenesisi245 – 2451R → D: Decreased spacer acquisition. 1 Publication
Mutagenesisi245 – 2451R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication
Mutagenesisi248 – 2481R → E: Dramatically decreased spacer acquisition in vivo. 1 Publication
Mutagenesisi252 – 2521R → A: No effect on spacer acquisition. 1 Publication
Mutagenesisi252 – 2521R → E: Loss of spacer acquisition, no Cas1-Cas2 complex formation, loss of CRISPR DNA-binding by complex. Protein is stable and dimerizes. 1 Publication
Mutagenesisi256 – 2594RSSK → ASSA: Loss of spacer acquisition in vivo. 1 Publication
Mutagenesisi256 – 2561R → A: No effect on spacer acquisition. 1 Publication
Mutagenesisi256 – 2561R → E: Loss of spacer acquisition. 1 Publication
Mutagenesisi282 – 30524Missing : No effect on spacer acquisition, Cas1-Cas2 complex formation or CRISPR DNA-binding by complex. 1 PublicationAdd
BLAST
Mutagenesisi291 – 2911I → G or R: No effect on spacer acquisition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305CRISPR-associated endonuclease Cas1PRO_0000169315Add
BLAST

Proteomic databases

PaxDbiQ46896.

Expressioni

Inductioni

Repressed by H-NS (PubMed:20132443). Activated by LeuO (PubMed:19429622). Activated by the BaeSR two-component regulatory system, possibly due to envelope stress (PubMed:21255106). Part of the casABCDE-ygbT-ygbF operon (PubMed:19429622).3 Publications

Interactioni

Subunit structurei

Homodimer (PubMed:21219465). Part of the Cas1-Cas2 complex (PubMed:24920831, PubMed:24793649, PubMed:25707795, Ref. 11, PubMed:26478180, PubMed:26503043). Interacts with RecB, RecC, RuvB, CasC and CasE (PubMed:21219465). Forms a hexamer with 2 Cas1 dimers sandwiching a Cas2 dimer (PubMed:24793649, PubMed:26478180). The DNA lies across a flat surface extending from 1 Cas1 dimer, across the Cas2 dimer and contacting the other Cas1 dimer. Only 1 Cas1 protein from each dimer is catalytic, the other interacts with the Cas2 dimer and possibly target DNA (PubMed:26478180, PubMed:26503043).1 Publication6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
yedVP763393EBI-1130209,EBI-554869

Protein-protein interaction databases

BioGridi4261582. 279 interactions.
DIPiDIP-12118N.
IntActiQ46896. 15 interactions.
STRINGi511145.b2755.

Structurei

Secondary structure

1
305
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Beta strandi17 – 204Combined sources
Beta strandi22 – 287Combined sources
Beta strandi31 – 366Combined sources
Beta strandi37 – 393Combined sources
Beta strandi41 – 433Combined sources
Helixi46 – 483Combined sources
Beta strandi50 – 545Combined sources
Beta strandi58 – 603Combined sources
Helixi62 – 709Combined sources
Beta strandi74 – 796Combined sources
Helixi80 – 823Combined sources
Beta strandi85 – 906Combined sources
Helixi95 – 10713Combined sources
Helixi109 – 12416Combined sources
Beta strandi130 – 1323Combined sources
Helixi134 – 15623Combined sources
Helixi167 – 1693Combined sources
Helixi170 – 1723Combined sources
Helixi175 – 19723Combined sources
Beta strandi206 – 2083Combined sources
Helixi214 – 22310Combined sources
Turni224 – 2274Combined sources
Helixi228 – 23811Combined sources
Helixi243 – 25816Combined sources
Helixi260 – 27314Combined sources
Beta strandi275 – 2773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NKDX-ray1.95A/B1-305[»]
3NKEX-ray1.40A/B/C92-291[»]
4P6IX-ray2.30C/D/E/F1-305[»]
4QDLX-ray2.70A/B/C/D1-305[»]
5DLJX-ray2.60A/B/C/D2-281[»]
5DQTX-ray3.10A/B/C/D/I/J/K/L1-305[»]
5DQUX-ray4.50A/B/C/D1-305[»]
5DQZX-ray2.70A/B/C/D1-305[»]
5DS4X-ray3.20A/B/C/D1-305[»]
5DS5X-ray2.95A/B/C/D1-305[»]
5DS6X-ray3.35A/B/C/D1-305[»]
ProteinModelPortaliQ46896.
SMRiQ46896. Positions 12-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 278183Sufficient for cleavage of ssRNA, ssDNA and Holliday junction DNAAdd
BLAST

Domaini

Substrate DNA-binding induces large structural changes that generate a surface for DNA-binding across the Cas2 dimer and formation of an optimal catalytic site (PubMed:26478180).1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105TZK. Bacteria.
COG1518. LUCA.
HOGENOMiHOG000015862.
InParanoidiQ46896.
KOiK15342.
OMAiIGDAGHR.
OrthoDBiEOG60PHDG.

Family and domain databases

HAMAPiMF_01470. Cas1.
InterProiIPR002729. CRISPR-assoc_Cas1.
IPR019851. CRISPR-assoc_Cas1_ECOLI.
[Graphical view]
PfamiPF01867. Cas_Cas1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00287. cas1. 2 hits.
TIGR03638. cas1_ECOLI. 1 hit.

Sequencei

Sequence statusi: Complete.

Q46896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTWLPLNPIP LKDRVSMIFL QYGQIDVIDG AFVLIDKTGI RTHIPVGSVA
60 70 80 90 100
CIMLEPGTRV SHAAVRLAAQ VGTLLVWVGE AGVRVYASGQ PGGARSDKLL
110 120 130 140 150
YQAKLALDED LRLKVVRKMF ELRFGEPAPA RRSVEQLRGI EGSRVRATYA
160 170 180 190 200
LLAKQYGVTW NGRRYDPKDW EKGDTINQCI SAATSCLYGV TEAAILAAGY
210 220 230 240 250
APAIGFVHTG KPLSFVYDIA DIIKFDTVVP KAFEIARRNP GEPDREVRLA
260 270 280 290 300
CRDIFRSSKT LAKLIPLIED VLAAGEIQPP APPEDAQPVA IPLPVSLGDA

GHRSS
Length:305
Mass (Da):33,194
Last modified:November 1, 1996 - v1
Checksum:i01A31BA98453D8A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29579 Genomic DNA. Translation: AAA69265.1.
U00096 Genomic DNA. Translation: AAC75797.1.
AP009048 Genomic DNA. Translation: BAE76832.1.
PIRiG65056.
RefSeqiNP_417235.1. NC_000913.3.
WP_000220066.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75797; AAC75797; b2755.
BAE76832; BAE76832; BAE76832.
GeneIDi947228.
KEGGiecj:JW2725.
eco:b2755.
PATRICi32120920. VBIEscCol129921_2852.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29579 Genomic DNA. Translation: AAA69265.1.
U00096 Genomic DNA. Translation: AAC75797.1.
AP009048 Genomic DNA. Translation: BAE76832.1.
PIRiG65056.
RefSeqiNP_417235.1. NC_000913.3.
WP_000220066.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NKDX-ray1.95A/B1-305[»]
3NKEX-ray1.40A/B/C92-291[»]
4P6IX-ray2.30C/D/E/F1-305[»]
4QDLX-ray2.70A/B/C/D1-305[»]
5DLJX-ray2.60A/B/C/D2-281[»]
5DQTX-ray3.10A/B/C/D/I/J/K/L1-305[»]
5DQUX-ray4.50A/B/C/D1-305[»]
5DQZX-ray2.70A/B/C/D1-305[»]
5DS4X-ray3.20A/B/C/D1-305[»]
5DS5X-ray2.95A/B/C/D1-305[»]
5DS6X-ray3.35A/B/C/D1-305[»]
ProteinModelPortaliQ46896.
SMRiQ46896. Positions 12-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261582. 279 interactions.
DIPiDIP-12118N.
IntActiQ46896. 15 interactions.
STRINGi511145.b2755.

Proteomic databases

PaxDbiQ46896.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75797; AAC75797; b2755.
BAE76832; BAE76832; BAE76832.
GeneIDi947228.
KEGGiecj:JW2725.
eco:b2755.
PATRICi32120920. VBIEscCol129921_2852.

Organism-specific databases

EchoBASEiEB2915.
EcoGeneiEG13114. ygbT.

Phylogenomic databases

eggNOGiENOG4105TZK. Bacteria.
COG1518. LUCA.
HOGENOMiHOG000015862.
InParanoidiQ46896.
KOiK15342.
OMAiIGDAGHR.
OrthoDBiEOG60PHDG.

Enzyme and pathway databases

BioCyciEcoCyc:G7425-MONOMER.
ECOL316407:JW2725-MONOMER.

Miscellaneous databases

PROiQ46896.

Family and domain databases

HAMAPiMF_01470. Cas1.
InterProiIPR002729. CRISPR-assoc_Cas1.
IPR019851. CRISPR-assoc_Cas1_ECOLI.
[Graphical view]
PfamiPF01867. Cas_Cas1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00287. cas1. 2 hits.
TIGR03638. cas1_ECOLI. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Involvement of the leucine response transcription factor LeuO in regulation of the genes for sulfa drug efflux."
    Shimada T., Yamamoto K., Ishihama A.
    J. Bacteriol. 191:4562-4571(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: OPERON STRUCTURE, INDUCTION BY LEUO.
    Strain: K12 / BW25113.
  4. "Identification and characterization of E. coli CRISPR-cas promoters and their silencing by H-NS."
    Pul U., Wurm R., Arslan Z., Geissen R., Hofmann N., Wagner R.
    Mol. Microbiol. 75:1495-1512(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REPRESSION BY H-NS.
    Strain: K12.
  5. "Envelope stress is a trigger of CRISPR RNA-mediated DNA silencing in Escherichia coli."
    Perez-Rodriguez R., Haitjema C., Huang Q., Nam K.H., Bernardis S., Ke A., DeLisa M.P.
    Mol. Microbiol. 79:584-599(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY BAER, ROLE IN PLASMID SILENCING, DISRUPTION PHENOTYPE.
    Strain: K12 / BW25113.
  6. "Detection and characterization of spacer integration intermediates in type I-E CRISPR-Cas system."
    Arslan Z., Hermanns V., Wurm R., Wagner R., Pul U.
    Nucleic Acids Res. 42:7884-7893(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A SPACER INTEGRASE, SUBUNIT, MUTAGENESIS OF ASP-221.
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Integrase-mediated spacer acquisition during CRISPR-Cas adaptive immunity."
    Nunez J.K., Lee A.S., Engelman A., Doudna J.A.
    Nature 519:193-198(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A SPACER INTEGRASE, PROBABLE REACTION MECHANISM, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-149; TYR-165; TYR-188; HIS-208; TYR-217; ASP-221 AND LYS-224.
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Intrinsic sequence specificity of the Cas1 integrase directs new spacer acquisition."
    Rollie C., Schneider S., Brinkmann A.S., Bolt E.L., White M.F.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR.
    Strain: K12 / MG1655 / ATCC 47076.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 92-291, FUNCTION AS AN ENDONUCLEASE, COFACTOR, ENZYME REGULATION, SUBUNIT, INTERACTION WITH RECB; RECC; RUVB; CASC AND CASE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-141; THR-184; TYR-188; HIS-208; LYS-211; ASP-218; ASP-221 AND LYS-224.
    Strain: K12.
  10. "Cas1-Cas2 complex formation mediates spacer acquisition during CRISPR-Cas adaptive immunity."
    Nunez J.K., Kranzusch P.J., Noeske J., Wright A.V., Davies C.W., Doudna J.A.
    Nat. Struct. Mol. Biol. 21:528-534(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CAS2, FUNCTION IN SPACER ACQUISITION, INTERACTION WITH CAS2 (YGBF), SUBUNIT, DNA-BINDING, MUTAGENESIS OF GLU-141; HIS-208; ASP-218; ASP-221; LYS-224; ARG-245; ARG-252; ARG-256; 282-PRO--SER-305 AND ILE-291.
    Strain: K12 / MG1655 / ATCC 47076.
  11. "Crystal structure of E.coli Cas1-Cas2 complex."
    Tamulaitiene G., Sinkunas T., Silanskas A., Gasiunas G., Grazulis S., Siksnys V.
    Submitted (MAY-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH CAS2, SUBUNIT.
  12. "Structural and mechanistic basis of PAM-dependent spacer acquisition in CRISPR-Cas systems."
    Wang J., Li J., Zhao H., Sheng G., Wang M., Yin M., Wang Y.
    Cell 163:840-853(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-281 IN COMPLEX WITH CAS2 AND DNA, FUNCTION, PROBABLE ACTIVE SITE, SUBUNIT, DOMAIN, DNA-BINDING, MUTAGENESIS OF TYR-22; ARG-59; ARG-84; TYR-165; TRP-170; TYR-188; HIS-208; TYR-217; 245-ARG--ARG-248 AND 256-ARG--LYS-259.
    Strain: K12.
  13. "Foreign DNA capture during CRISPR-Cas adaptive immunity."
    Nunez J.K., Harrington L.B., Kranzusch P.J., Engelman A.N., Doudna J.A.
    Nature 527:535-538(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CAS2 AND DNA, FUNCTION, PROBABLE ACTIVE SITE, SUBUNIT, DNA-BINDING, MUTAGENESIS OF TYR-22; ARG-41; ARG-59; ARG-66; ARG-84; ARG-245 AND ARG-248.

Entry informationi

Entry nameiCAS1_ECOLI
AccessioniPrimary (citable) accession number: Q46896
Secondary accession number(s): Q2MA74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.